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3TMK

CRYSTAL STRUCTURE OF YEAST THYMIDYLATE KINASE COMPLEXED WITH THE BISUBSTRATE INHIBITOR TP5A AT 2.0 A RESOLUTION: IMPLICATIONS FOR CATALYSIS AND AZT ACTIVATION

Summary for 3TMK
Entry DOI10.2210/pdb3tmk/pdb
DescriptorTHYMIDYLATE KINASE, P1-(5'-ADENOSYL)P5-(5'-THYMIDYL)PENTAPHOSPHATE (3 entities in total)
Functional Keywordskinase, phosphotransferase
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Total number of polymer chains8
Total formula weight204885.83
Authors
Lavie, A.,Schlichting, I.,Konrad, M.,Goody, R.S.,Brundiers, R.,Reinstein, J. (deposition date: 1998-01-26, release date: 1999-02-16, Last modification date: 2023-08-09)
Primary citationLavie, A.,Konrad, M.,Brundiers, R.,Goody, R.S.,Schlichting, I.,Reinstein, J.
Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation.
Biochemistry, 37:3677-3686, 1998
Cited by
PubMed: 9521686
DOI: 10.1021/bi9720787
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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